Rapid determination and NMR assignments of antiparallel sheets and helices of a scorpion and a cobra toxin.
An NMR method is described which should provide a rapid means for determining and assigning antiparallel sheets and helices in small proteins. It begins by locating apparent NOESY crosspeaks which suggest the presence of the secondary structure; this is followed by searches for MCD patterns (Englander & Wand (1987) Biochemistry 22, 5953) which are characteristic of these structures. As a result, only spin-systems of the amino acids within the secondary structure need to be defined. A triple-stranded, antiparallel sheet and a helix have been found and assigned for both alpha-cobratoxin and the scorpion toxin AaH III.
Laplante
S R
SR
Institute of Natural Substances Chemistry, CNRS, Gif-sur-Yvette, France.
Mikou
A
A
Robin
M
M
Guittet
E
E
Delsuc
M A
MA
Charpentier
I
I
Lallemand
J Y
JY
D000818:Animals; D003039:Cobra Neurotoxin Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D015394:Molecular Structure; D009479:Neuropeptides / Q000737:chemistry*; D011487:Protein Conformation; D012604:Scorpion Venoms
D003039:Cobra Neurotoxin Proteins; D009479:Neuropeptides; D012604:Scorpion Venoms; C067223:scorpion toxin AaH III; C025154:alpha-cobratoxin